scholarly journals The Nodulation Factor Hydrolase of Medicago truncatula: Characterization of an Enzyme Specifically Cleaving Rhizobial Nodulation Signals

2013 ◽  
Vol 163 (3) ◽  
pp. 1179-1190 ◽  
Author(s):  
Ye Tian ◽  
Wei Liu ◽  
Jie Cai ◽  
Lan-Yue Zhang ◽  
Kam-Bo Wong ◽  
...  
2019 ◽  
pp. 1006-1014
Author(s):  
Gyöngyi Zs. Kontra‐Kováts ◽  
Lili Fodor ◽  
Beatrix Horváth ◽  
Ágota Domonkos ◽  
Gergely Iski ◽  
...  

2014 ◽  
Vol 32 (5) ◽  
pp. 1030-1040 ◽  
Author(s):  
Ángel M. Villegas-Fernández ◽  
Franziska Krajinski ◽  
Armin Schlereth ◽  
Eva Madrid ◽  
Diego Rubiales

Author(s):  
M. Ángeles Castillejo ◽  
Mónica Fernández‐Aparicio ◽  
Diego Rubiales

2019 ◽  
Vol 300 ◽  
pp. 32-39 ◽  
Author(s):  
Li Gao ◽  
Ye Tian ◽  
Meng-Ci Chen ◽  
Li Wei ◽  
Tian-Ge Gao ◽  
...  

BMC Genomics ◽  
2019 ◽  
Vol 20 (1) ◽  
Author(s):  
Hongfeng Wang ◽  
Zhichao Lu ◽  
Yiteng Xu ◽  
Lingcui Kong ◽  
Jianjun Shi ◽  
...  

2003 ◽  
Vol 133 (4) ◽  
pp. 1893-1910 ◽  
Author(s):  
Maria-Téresa Navarro-Gochicoa ◽  
Sylvie Camut ◽  
Antonius C.J. Timmers ◽  
Andreas Niebel ◽  
Christine Hervé ◽  
...  

2011 ◽  
Vol 62 (15) ◽  
pp. 5595-5605 ◽  
Author(s):  
M.-C. Morere-Le Paven ◽  
L. Viau ◽  
A. Hamon ◽  
C. Vandecasteele ◽  
A. Pellizzaro ◽  
...  

2006 ◽  
Vol 395 (3) ◽  
pp. 641-652 ◽  
Author(s):  
Richard K. Hughes ◽  
Eric J. Belfield ◽  
Mylrajan Muthusamay ◽  
Anuja Khan ◽  
Arthur Rowe ◽  
...  

We describe the detailed biochemical characterization of CYP74C3 (cytochrome P450 subfamily 74C3), a recombinant plant cytochrome P450 enzyme with HPL (hydroperoxide lyase) activity from Medicago truncatula (barrel medic). Steady-state kinetic parameters, substrate and product specificities, RZ (Reinheitszahl or purity index), molar absorption coefficient, haem content, and new ligands for an HPL are reported. We show on the basis of gel filtration, sedimentation velocity (sedimentation coefficient distribution) and sedimentation equilibrium (molecular mass) analyses that CYP74C3 has low enzyme activity as a detergent-free, water-soluble, monomer. The enzyme activity can be completely restored by re-activation with detergent micelles, but not detergent monomers. Corresponding changes in the spin state equilibrium, and probably co-ordination of the haem iron, are novel for cytochrome P450 enzymes and suggest that detergent micelles have a subtle effect on protein conformation, rather than substrate presentation, which is sufficient to improve substrate binding and catalytic-centre activity by an order of magnitude. The kcat/Km of up to 1.6×108 M−1·s−1 is among the highest recorded, which is remarkable for an enzyme whose reaction mechanism involves the scission of a C–C bond. We carried out both kinetic and biophysical studies to demonstrate that this effect is a result of the formation of a complex between a protein monomer and a single detergent micelle. Association with a detergent micelle rather than oligomeric state represents a new mechanism of activation for membrane-associated cytochrome P450 enzymes. Highly concentrated and monodispersed samples of detergent-free CYP74C3 protein may be well suited for the purposes of crystallization and structural resolution of the first plant cytochrome P450 enzyme.


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